Physical Principles and Techniques of Protein Chemistry, Part 1 |
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Page 144
products of hydrolysis. Binding of DDS to serum albumin produces a negative
difference spectrum in the 280–310 mp region (Fig. 17), resulting mainly or
entirely from a blue shift in the spectrum of the 2 indole and 21 phenolic
chromophores, ...
products of hydrolysis. Binding of DDS to serum albumin produces a negative
difference spectrum in the 280–310 mp region (Fig. 17), resulting mainly or
entirely from a blue shift in the spectrum of the 2 indole and 21 phenolic
chromophores, ...
Page 237
shift in the emission peak on binding of ANS, a similar trend was observed when
ANS was dissolved in a series of aliphatic alcohols of increasing chain length.
The quantum yield and emission peak of ANS in n-octanol are 0.63 and 464 mp ...
shift in the emission peak on binding of ANS, a similar trend was observed when
ANS was dissolved in a series of aliphatic alcohols of increasing chain length.
The quantum yield and emission peak of ANS in n-octanol are 0.63 and 464 mp ...
Page 526
Ribonuclease chromophores in, exposure of, 144–145 conformation changes in,
by fluorescence, 226–227, 229 2'-cytidylic acid binding by, 491 denaturation of
difference spectra for, 136–139 rates of, 280, 288 difference spectra of, ...
Ribonuclease chromophores in, exposure of, 144–145 conformation changes in,
by fluorescence, 226–227, 229 2'-cytidylic acid binding by, 491 denaturation of
difference spectra for, 136–139 rates of, 280, 288 difference spectra of, ...
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Contents
Electron Microscopy | 2 |
Dielectric Properties of Proteins | 7 |
Operational Requirements for HighResolution Electron | 15 |
Copyright | |
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absorbance absorption acid albumin appears applied atoms axis binding birefringence boundary buffer calculated cell charge Chem chromophores concentration constant containing contrast corrected corresponding curve dependence determined dielectric difference diffusion dipole direction effect electric electric field electron electrophoresis emission energy equation equilibrium example excitation experimental experiments factor field flow fluorescence fraction frequency function given groups important increase indicates intensity interactions ionic ions length light limited macromolecules measured method microscope mobility molecular molecules observed obtained occurs optical particles patterns peaks perturbation phase polarization position possible preparation present produced protein range ratio reaction reference relative relaxation resolution respectively rotation sample separation serum shift shown single solution solvent specimen spectra spectrum strength structure studies technique temperature theory tion tryptophan unit usually values volume wavelength weight yield zone